ID TFB3_YEAST Reviewed; 321 AA. AC Q03290; D6VT84; P89104; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-SEP-2023, entry version 189. DE RecName: Full=RNA polymerase II transcription factor B subunit 3; DE AltName: Full=RNA polymerase II transcription factor B 38 kDa subunit; DE AltName: Full=RNA polymerase II transcription factor B p38 subunit; GN Name=TFB3; Synonyms=RIG2; OrderedLocusNames=YDR460W; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 71-85 AND 236-250, RP FUNCTION, SUBUNIT, AND INTERACTION WITH KIN28. RC STRAIN=DBY2019; RX PubMed=9235928; DOI=10.1074/jbc.272.31.19319; RA Feaver W.J., Henry N.L., Wang Z., Wu X., Svejstrup J.Q., Bushnell D.A., RA Friedberg E.C., Kornberg R.D.; RT "Genes for Tfb2, Tfb3, and Tfb4 subunits of yeast transcription/repair RT factor IIH. Homology to human cyclin-dependent kinase activating kinase and RT IIH subunits."; RL J. Biol. Chem. 272:19319-19327(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT. RX PubMed=9294030; DOI=10.1007/s004380050518; RA Faye G., Simon M., Valay J.G., Fesquet D., Facca C.; RT "Rig2, a RING finger protein that interacts with the Kin28/Ccl1 CTD kinase RT in yeast."; RL Mol. Gen. Genet. 255:460-466(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [4] RP SEQUENCE REVISION. RC STRAIN=ATCC 204508 / S288c; RA Sethuraman A., Cherry J.M.; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [6] RP IDENTIFICATION IN A COMPLEX WITH KIN28 AND CCL1. RX PubMed=11839796; DOI=10.1128/mcb.22.5.1288-1297.2002; RA Keogh M.-C., Cho E.-J., Podolny V., Buratowski S.; RT "Kin28 is found within TFIIH and a Kin28-Ccl1-Tfb3 trimer complex with RT differential sensitivities to T-loop phosphorylation."; RL Mol. Cell. Biol. 22:1288-1297(2002). RN [7] RP SUBUNIT. RX PubMed=14500720; DOI=10.1074/jbc.c300417200; RA Takagi Y., Komori H., Chang W.-H., Hudmon A., Erdjument-Bromage H., RA Tempst P., Kornberg R.D.; RT "Revised subunit structure of yeast transcription factor IIH (TFIIH) and RT reconciliation with human TFIIH."; RL J. Biol. Chem. 278:43897-43900(2003). RN [8] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-258, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157 AND THR-258, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). CC -!- FUNCTION: Acts as component of the general transcription and DNA repair CC factor IIH (TFIIH or factor B), which is essential for both basal and CC activated transcription, and is involved in nucleotide excision repair CC (NER) of damaged DNA. TFIIH has CTD kinase and DNA-dependent ATPase CC activity, and is essential for polymerase II transcription in vitro. CC {ECO:0000269|PubMed:9235928, ECO:0000269|PubMed:9294030}. CC -!- SUBUNIT: Component of the transcription factor IIH (TFIIH) holo but not CC the TFIIH core complex. Component of a complex consisting of KIN28, CC CCL1 and TFB3; the KIN28-CCL1 dimer is known as the TFIIK complex. CC {ECO:0000269|PubMed:11839796, ECO:0000269|PubMed:14500720, CC ECO:0000269|PubMed:9235928, ECO:0000269|PubMed:9294030}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- MISCELLANEOUS: Present with 3050 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB40629.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U62805; AAB40629.1; ALT_FRAME; Genomic_DNA. DR EMBL; U33050; AAB64899.1; -; Genomic_DNA. DR EMBL; BK006938; DAA12294.1; -; Genomic_DNA. DR PIR; S69628; S69628. DR RefSeq; NP_010748.3; NM_001180768.3. DR PDB; 5OQJ; EM; 4.70 A; 3=1-321. DR PDB; 5OQM; EM; 5.80 A; 3=1-321. DR PDB; 6GYM; EM; 6.70 A; 3=1-321. DR PDB; 6XI8; EM; 3.64 A; C=259-321. DR PDB; 7KUE; EM; 3.50 A; C=1-321. DR PDB; 7ML0; EM; 3.00 A; 3=1-321. DR PDB; 7ML1; EM; 4.00 A; 3=1-321. DR PDB; 7ML2; EM; 3.40 A; 3=1-321. DR PDB; 7ML3; EM; 7.60 A; 3=1-321. DR PDB; 7ML4; EM; 3.10 A; 3=1-321. DR PDB; 7O4I; EM; 3.20 A; 3=1-321. DR PDB; 7O4J; EM; 2.90 A; 3=1-321. DR PDB; 7O4K; EM; 3.60 A; 3=1-321. DR PDB; 7O4L; EM; 3.40 A; 3=1-321. DR PDB; 7O72; EM; 3.40 A; 3=1-321. DR PDB; 7O73; EM; 3.40 A; 3=1-321. DR PDB; 7O75; EM; 3.20 A; 3=1-321. DR PDB; 7ZS9; EM; 3.10 A; 3=1-321. DR PDB; 7ZSA; EM; 4.00 A; 3=1-321. DR PDB; 7ZSB; EM; 6.60 A; 3=1-321. DR PDBsum; 5OQJ; -. DR PDBsum; 5OQM; -. DR PDBsum; 6GYM; -. DR PDBsum; 6XI8; -. DR PDBsum; 7KUE; -. DR PDBsum; 7ML0; -. DR PDBsum; 7ML1; -. DR PDBsum; 7ML2; -. DR PDBsum; 7ML3; -. DR PDBsum; 7ML4; -. DR PDBsum; 7O4I; -. DR PDBsum; 7O4J; -. DR PDBsum; 7O4K; -. DR PDBsum; 7O4L; -. DR PDBsum; 7O72; -. DR PDBsum; 7O73; -. DR PDBsum; 7O75; -. DR PDBsum; 7ZS9; -. DR PDBsum; 7ZSA; -. DR PDBsum; 7ZSB; -. DR AlphaFoldDB; Q03290; -. DR SMR; Q03290; -. DR BioGRID; 32514; 39. DR ComplexPortal; CPX-1659; General transcription factor complex TFIIH. DR ComplexPortal; CPX-1660; General transcription factor complex TFIIK. DR DIP; DIP-2398N; -. DR IntAct; Q03290; 16. DR MINT; Q03290; -. DR STRING; 4932.YDR460W; -. DR iPTMnet; Q03290; -. DR MaxQB; Q03290; -. DR PaxDb; Q03290; -. DR PeptideAtlas; Q03290; -. DR EnsemblFungi; YDR460W_mRNA; YDR460W; YDR460W. DR GeneID; 852071; -. DR KEGG; sce:YDR460W; -. DR AGR; SGD:S000002868; -. DR SGD; S000002868; TFB3. DR VEuPathDB; FungiDB:YDR460W; -. DR eggNOG; KOG3800; Eukaryota. DR GeneTree; ENSGT00390000002319; -. DR HOGENOM; CLU_048466_1_1_1; -. DR InParanoid; Q03290; -. DR OMA; REYYSRT; -. DR OrthoDB; 9088at2759; -. DR BioCyc; YEAST:G3O-29988-MONOMER; -. DR Reactome; R-SCE-113418; Formation of the Early Elongation Complex. DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex. DR Reactome; R-SCE-6782135; Dual incision in TC-NER. DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER. DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes. DR Reactome; R-SCE-69202; Cyclin E associated events during G1/S transition. DR Reactome; R-SCE-72086; mRNA Capping. DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape. DR Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape. DR Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening. DR Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation. DR Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance. DR Reactome; R-SCE-77075; RNA Pol II CTD phosphorylation and interaction with CE. DR BioGRID-ORCS; 852071; 0 hits in 10 CRISPR screens. DR PRO; PR:Q03290; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; Q03290; Protein. DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IDA:SGD. DR GO; GO:0070985; C:transcription factor TFIIK complex; IDA:SGD. DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IBA:GO_Central. DR GO; GO:0006289; P:nucleotide-excision repair; IDA:ComplexPortal. DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:InterPro. DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:ComplexPortal. DR CDD; cd16573; RING-HC_TFB3-like; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR015877; Cdk-activating_kinase_MAT1_cen. DR InterPro; IPR004575; MAT1/Tfb3. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR NCBIfam; TIGR00570; cdk7; 1. DR PANTHER; PTHR12683; CDK-ACTIVATING KINASE ASSEMBLY FACTOR MAT1; 1. DR PANTHER; PTHR12683:SF13; CDK-ACTIVATING KINASE ASSEMBLY FACTOR MAT1; 1. DR Pfam; PF06391; MAT1; 1. DR Pfam; PF17121; zf-C3HC4_5; 1. DR PIRSF; PIRSF003338; MAT1_metazoa; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..321 FT /note="RNA polymerase II transcription factor B subunit 3" FT /id="PRO_0000055942" FT ZN_FING 13..60 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT MOD_RES 157 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 258 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956" FT TURN 14..16 FT /evidence="ECO:0007829|PDB:7O4J" FT TURN 20..22 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 28..30 FT /evidence="ECO:0007829|PDB:7O4J" FT TURN 32..34 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 37..39 FT /evidence="ECO:0007829|PDB:7O75" FT HELIX 40..47 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:7ML0" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:7ML2" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:7ML0" FT HELIX 76..89 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 92..94 FT /evidence="ECO:0007829|PDB:7ML0" FT HELIX 96..99 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 103..122 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 126..138 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 262..265 FT /evidence="ECO:0007829|PDB:7KUE" FT TURN 280..284 FT /evidence="ECO:0007829|PDB:7KUE" FT HELIX 285..287 FT /evidence="ECO:0007829|PDB:7KUE" FT HELIX 289..292 FT /evidence="ECO:0007829|PDB:7KUE" FT TURN 293..295 FT /evidence="ECO:0007829|PDB:7KUE" FT HELIX 298..308 FT /evidence="ECO:0007829|PDB:7KUE" FT TURN 309..312 FT /evidence="ECO:0007829|PDB:7KUE" SQ SEQUENCE 321 AA; 38128 MW; 528D61CF25ADFAF4 CRC64; MLMDEYEENK DMCPICKTDR YLSPDVKFLV NPECYHRICE SCVDRIFSLG PAQCPYKGCD KILRKNKFKT QIFDDVEVEK EVDIRKRVFN VFNKTIDDFN GDLVEYNKYL EEVEDIIYKL DHGIDVAKTE EKLRTYEELN KQLIMNNLER SRTEIESFEQ RQKFEKEMKL KKRLLERQIE EEERMNKEWT KKEIVNRLST TTQDINETIE GVKNTVKLKK SSARRKLEEL NRVLKNNPYF NSNVNVQNSR LKDAVPFTPF NGDREAHPRF TLKGSVYNDP FIKDLEHRKE FIASGFNTNY AYERVLTEAF MGLGCVISEE L //